Publications: protein design, synthetic biology

Link to All papers

Selected Regan publications.

Protein-Based Materials and Surfaces.

Facile protein immobilization using engineered suface-active biofilm proteins. 

Danielle M. Williams, Gilad Kaufman, Hadi Izadi, Abigail E. Gahm, Sarah M. Prophet, Kyle T. Vanderlick, Chinedum O. Osuji and Lynne Regan.

ACS Applied Nano Materials 2018 1:2483–2488

Here we use a combination of natural proteins with unusual physical properties (BslA1, SpyCatcher/SpyTag, SnoopCatcher/SnoopTag) to create surfaces to present and display a variety of proteins. This work is important because for biosensor applications, the ability to present a protein on a surface, whilst simultaneously preventing both its interaction with that surface and the non-specific binding of analytes to the surface, is vital.  

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Fabrication of modularly functionalizable microcapsules using protein-based technologies.BslA

Ashley C. Schloss, Wei Liu, Danielle M. Williams, Gilad Kaufman, Heidi P. Hendrickson, Benjamin Rudshteyn, Li Fu, Hongfei Wang, Victor S. Batista, Chinedum Osuji, Elsa C. Y. Yan and Lynne Regan.

ACS Biomaterials Science and Engineering 2016 2:1856-1861.

Here we use microfluidics to create oil in water microcapsules and use a combination of natural proteins with unusual physical properties (BslA1, SpyCatcher/SpyTag, SnoopCatcher/SnoopTag) to functionalise them. This work is important because such microcapsules could be used to deliver water-insoluble drugs, and by functionalization target their delivery to the desired cells. 

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Stimuli-responsive smart gels realized via modular protein design.

Tijana Z. Grove, Chinedum O. Osuji, Jason D. Forster, Eric R. Dufresne and Lynne Regan.

ASC Journal of the American Chemical Society 2010 132:14024-6.

Here we use designed repeat protein arrays, in combination with multi-dentate peptide cross-linkers, to make stimuli-responsive hydrogels. These gels form and ‘dissolve’ reversibly in response to specific molecular stimuli. Moreover, their macroscopic viscoelastic properties are specified by the molecular details of their construction. This work is important because the ability to create gel matrices of user-prescribed stiffness is vital for many applications in tissue engineering and stem cell technologies. 

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Synthetic Proteins for Synthetic Biology: Interrogating, Illuminating and Modulating Cellular Processes using Designed Proteins.

A new method for post-translationally labeling proteins in live cells for fluorescence imaging and tracking.

Hinrichsen M, Lenz M, Edwards JM, Miller OK, Mochrie SGJ, Swain PS, Schwarz-Linek U, and Lynne Regan.

Protein Engineering, Design & Selection 2017 30:771-780.

Here we used a designed protein-peptide pair to covalently label proteins, post-translationally, in live cells. This work is important because labelling a protein when it is in its final, functional, state is less perturbing to its function, as we demonstrate.  We use our method, combined with microfluidics and single cell tracking, to study protein life-times in the plasma membrane of yeast (S. cerevisiae). 


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Designed proteins as novel imaging reagents in living Escherichia coli.

Susan E. Pratt, Elizabeth B. Speltz, Simon G. J. Mochrie and Lynne Regan.

Chembiochem 2016 117:652-7.

Here we used designed protein-peptides to non-covalently label proteins in live cells. This work is important because we designed protein-peptide pairs of different affinities, (measured in vitro), and we then demonstrated how those different affinity pairs function in vivo, in live E. coli.

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Design of protein-peptide interaction modules for assembling supramolecular structures in vivo and in vitro.

Elizabeth B. Speltz, Aparna Nathan and Lynne Regan.

ACS Chemical Biology 2015 10:2108-15.

Here we designed protein modules that bind to short peptides. This work is important because the binding specificities of these modules are orthogonal to each other and to all yeast proteins. Thus, they can be used to assemble supramolecular structure, both in vitro and in vivo.

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Designed proteins to modulate cellular networks.

Aitziber L. Cortajarena, Tina Y. Liu, Mark Hochstrasser and Lynne Regan.

ACS Chemical Biology 2010 5:545-52.

Here we used a combination of design and selection to obtain protein modules that bind to a specific region of a cellular protein (SEM1). This work is important, because we showed that by expressing the protein modules in yeast, we can inhibit the function of SEM1, with clear phenotypic consequences.

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